ID A0A411WIK7_9GAMM Unreviewed; 336 AA.
AC A0A411WIK7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:QBH96023.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:QBH96023.1};
GN ORFNames=EKN56_06190 {ECO:0000313|EMBL:QBH96023.1};
OS Limnobaculum zhutongyuii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Limnobaculum.
OX NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH96023.1, ECO:0000313|Proteomes:UP000293154};
RN [1] {ECO:0000313|EMBL:QBH96023.1, ECO:0000313|Proteomes:UP000293154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF-458 {ECO:0000313|EMBL:QBH96023.1,
RC ECO:0000313|Proteomes:UP000293154};
RA Ge Y.;
RT "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; CP034752; QBH96023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WIK7; -.
DR KEGG; prag:EKN56_06190; -.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000293154; Chromosome.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR PIRSF; PIRSF000148; ASA_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:QBH96023.1}.
FT DOMAIN 6..121
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
SQ SEQUENCE 336 AA; 36274 MW; F721B40ACB991D7D CRC64;
MTDGWQVAVL GATGAVGEAL LELLQERNFP VGELYLLASE RTAGETLRFN GKSIVVQNAA
EFDWSQAQLA FFVAGAEAAV RYADEAANSG CLVIDNSGVF SLEPEVPLVV PGVNNHALAE
YRNRNIVAVA DSLTSQLLTA IKPLSEAAGL SRLQVTTMLS ASAHGKAAVD DLAGQSARLL
NGLPVEEGFF NKQLAFNLLP LLPDSEGSVR EERRMVDETR KVLQDEGLAI SISCIQSPVF
YGNAQVVHME GLRPVSAEEA YDELSNAEDI QLSENDDYPT QVGDATGNPH LSVGCLRNDY
GIPEQIQFWS VADNIRFGGA LMMVKTAESL TQEYFY
//
